ACL_RS07315


  Uniprot: A9NHB3
Description: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
EC number: 3.2.2.9
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. {ECO:0000256|SAAS:SAAS00035191}.; CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + H(2)O = S-methyl-5-thio-D-ribose + adenine. {ECO:0000256|SAAS:SAAS00035176}.
Cofactor: 
Enzyme regulation: 
Function [CC]: FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. {ECO:0000256|SAAS:SAAS00035153}.
Pathway: PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. {ECO:0000256|SAAS:SAAS00035194}.
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): pfs
Gene names (synonym): 
Mass: 23,547
Subunit structure [CC]: 
Gene ontology (GO): adenosylhomocysteine nucleosidase activity [GO:0008782]; methylthioadenosine nucleosidase activity [GO:0008930]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; nucleoside catabolic process [GO:0009164]
Gene ontology IDs: GO:0008782; GO:0008930; GO:0009164; GO:0019509
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN subfamily. {ECO:0000256|SAAS:SAAS00548801}.
Protein families: PNP/UDP phosphorylase family, MtnN subfamily
Coiled coil: 
Domain [FT]: DOMAIN 2 203 PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
Motif: 
Region: 
EMBL: CP000896
ProteinModelPortal: A9NHB3
MEROPS: 
EnsemblBacteria KO: ABX81743
UniPathway: K01243
CDD: 
Gene3D: 
HAMAP: 3.40.50.1580
InterPro: 
PANTHER: IPR010049;IPR018017;IPR000845
PIRSF: PTHR21234
PRINTS: 
PROSITE: 
Pfam: 
ProDom: PF01048
SMART: 
SUPFAM: 
TIGRFAMs: SSF53167
1197589-1198219(-)

>nucleotide sequence
TTAAATCACCTCTAATACTTGATCGAGTGCATCAATTAAAGCATTAGATAGTTCTGTTTC
ACTTTTTTTGTATACTTCCATTTGGTCATGACTACCTAATACATCGGATACTACTTTAAT
AGCTAATACAGGATATTTGTAGCTATGCGCTACTTGATAAATACTTGCACCTTCCATATC
CACGATATATGAATTTGGATTAATTGGTTTTGTAGAGAATATATCACCTGTGTATAATCT
GATTTGATTGAAATCTTCTAATTTATTTAGTATTTTAGTATCTGTAAAATAGAGTGTTGG
ATATTTAGGAATTTGTCCATATTCATAGTTAAATATCGTTAAATCCACATCATGGTAAGT
GACCTCAGATACCAGGTATGTATCATAAAGATTCACCTTATGTCCACCAACGATACCAAG
ATTGATTATAAATCTAGTTTCAGGATGCAATGTTAAGATATGTGATAGTGCACTAGATGC
ATTTGTTTTACCAATGCCAGAAATGATAAGCATCACATCTTGTCCCTGGTATTTACCCTC
ATATATGTTATAAGGGTGTGTTGATTTTAAGTTTAAATTGGAAGTAAGTACTTCTACTTC
AGATAGCATCGCTGCAATAATAACTATCAT


>protein sequence
MIVIIAAMLSEVEVLTSNLNLKSTHPYNIYEGKYQGQDVMLIISGIGKTNASSALSHILT
LHPETRFIINLGIVGGHKVNLYDTYLVSEVTYHDVDLTIFNYEYGQIPKYPTLYFTDTKI
LNKLEDFNQIRLYTGDIFSTKPINPNSYIVDMEGASIYQVAHSYKYPVLAIKVVSDVLGS
HDQMEVYKKSETELSNALIDALDQVLEVI






















© Fisunov Lab of Proteomics, 2016.